The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease
The structure was published by Orwig, S.D., Tan, Y.L., Grimster, N.P., et al., Powers, E.T., Kelly, J.W., and Lieberman, R.L., in 2011 in a paper entitled "Binding of 3,4,5,6-tetrahydroxyazepanes to the acid-beta-glucosidase active site: implications for pharmacological chaperone design for Gaucher disease" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.48 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Glucosylceramidase.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: